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4I9Z

Crystal structure of the PDE5A1 catalytic domain in complex with novel inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
A0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 5BA A 901
ChainResidue
AVAL548
AALA823
APEG904
AHOH1037
ATYR612
ALEU675
AALA779
AVAL782
APHE786
AMET816
AGLN817
APHE820

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 902
ChainResidue
AHIS617
AHIS653
AASP654
AASP764
AHOH1004
AHOH1138

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 903
ChainResidue
AASP654
AHOH1001
AHOH1002
AHOH1015
AHOH1137
AHOH1138

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 904
ChainResidue
AARG577
AGLY819
AASP822
AALA823
A5BA901
AHOH1025
AHOH1049

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG A 905
ChainResidue
ASER562
APHE564
AGLU565
ALEU690
AASN694
ATYR709
APRO773
AARG777
AHOH1052

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGvnNsY
ChainResidueDetails
AHIS653-TYR664

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083
ChainResidueDetails
AHIS613

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12955149, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1T9R, ECO:0007744|PDB:1T9S, ECO:0007744|PDB:1TBF
ChainResidueDetails
AASP654
AASP764
AHIS617
AHIS653

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12955149
ChainResidueDetails
AGLN817

221051

PDB entries from 2024-06-12

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